dbPTM

LRP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LRP6_HUMAN
UniProt AC	O75581
Protein Name	Low-density lipoprotein receptor-related protein 6
Gene Name	LRP6
Organism	Homo sapiens (Human).
Sequence Length	1613
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Endoplasmic reticulum . Membrane raft . On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on pa
Protein Description	Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalsomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalsomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity)..
Protein Sequence	MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKRTEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEGLREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLLENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGKIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATNVHRVIGSNPCAEENGGCSHLCLYRPQGLRCACPIGFELISDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSNMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQSGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPTTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNMIRKAQEDGSQGFTVVVSSVPSQNLEIQPYDLSIDIYSRYIYWTCEATNVINVTRLDGRSVGVVLKGEQDRPRAVVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSRLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGEIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCIGKHKKCDHNVDCSDKSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTVYFICQRMLCPRMKGDGETMTNDYVVHGPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDLNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	N-linked_Glycosylation	DATNGKENATIVVGG ECCCCCCCEEEEECC	45.96	UniProtKB CARBOHYD
81	N-linked_Glycosylation	AIKRTEFNKTESVQN HHHHCCCCCCHHCCE	44.07	UniProtKB CARBOHYD
108	Ubiquitination	ACDWLGEKLYWTDSE CCCCCCCCEEECCCC	45.11	-
122	Phosphorylation	ETNRIEVSNLDGSLR CCCEEEEECCCCHHH	20.91	20230923
127	Phosphorylation	EVSNLDGSLRKVLFW EEECCCCHHHHEEEE	25.35	20230923
171	Phosphorylation	ERAGMDGSSRFIIIN EECCCCCCCEEEEEC	17.67	-
172	Phosphorylation	RAGMDGSSRFIIINS ECCCCCCCEEEEECC	36.42	-
179	Phosphorylation	SRFIIINSEIYWPNG CEEEEECCEEECCCC	18.24	28787133
188	Phosphorylation	IYWPNGLTLDYEEQK EECCCCCCCCHHHHH	20.98	28787133
209	Phosphorylation	KLNFIHKSNLDGTNR HCCEEECCCCCCCCC	28.58	-
214	Phosphorylation	HKSNLDGTNRQAVVK ECCCCCCCCCEEEHH	27.22	-
281	N-linked_Glycosylation	FSQQRQPNATNPCGI HCCCCCCCCCCCCCC	51.57	UniProtKB CARBOHYD
322	Phosphorylation	KLLENGKTCKDGATE EECCCCCCCCCCHHH	26.62	30576142
328	Phosphorylation	KTCKDGATELLLLAR CCCCCCHHHHHHHHH	32.47	30576142
418	Phosphorylation	DWVARNLYWTDTGTD EEEHHHEECCCCCCC	15.15	22210691
420	Phosphorylation	VARNLYWTDTGTDRI EHHHEECCCCCCCEE	15.32	22210691
433	N-linked_Glycosylation	RIEVTRLNGTMRKIL EEEEEEECCCEEEEE	40.37	UniProtKB CARBOHYD
486	N-linked_Glycosylation	SDRVVLVNTSLGWPN CCEEEEEECCCCCCC	21.57	UniProtKB CARBOHYD
646	Phosphorylation	RADIRRISLETNNNN CCCCEEEEEECCCCC	20.52	26091039
692	N-linked_Glycosylation	TISRAFMNGSALEHV HHHHHHHCCHHHHHH	34.51	22000856
709	Ubiquitination	FGLDYPEGMAVDWLG CCCCCCCCCCEEECC	12.58	22817900
733	Ubiquitination	TNRIEVSKLDGQHRQ CCEEEEEECCCCCCE	56.63	29967540
802	Acetylation	GLTIDYAKRRLYWTD CCEEEHHHHEEEEEC	31.64	7972595
826	Ubiquitination	NMLGLNREVIADDLP CCCCCCCEEECCCCC	36.88	22817900
859	N-linked_Glycosylation	RRSIERANKTSGQNR HHHHHHHHCCCCCCC	55.12	22000856
865	N-linked_Glycosylation	ANKTSGQNRTIIQGH HHCCCCCCCEEEEHH	46.73	22000856
926	N-linked_Glycosylation	HYSLNADNRTCSAPT CEECCCCCCEECCCC	38.46	22000856
941	Ubiquitination	TFLLFSQKSAINRMV EEEEEECCCHHHHHC	40.43	-
963	Phosphorylation	DIILPIHSLRNVRAI CEEEEHHHCCCCCCC	29.73	24719451
977	Ubiquitination	IDYDPLDKQLYWIDS CCCCCCCCEEEEEHH	50.30	21906983
1001	Phosphorylation	EDGSQGFTVVVSSVP HCCCCCEEEEEECCC	21.15	-
1025	Phosphorylation	DLSIDIYSRYIYWTC EEEEEEEECEEEEEE	20.95	24719451
1039	N-linked_Glycosylation	CEATNVINVTRLDGR ECCCCEEEEEECCCC	25.48	22000856
1175	Ubiquitination	EKIDMTGREGRTKVQ HHCCCCCCCCHHHHH	33.75	23000965
1195	Ubiquitination	LSDIHAVKELNLQEY HHHHHHHHCCCHHHH	58.21	29967540
1209	Ubiquitination	YRQHPCAQDNGGCSH HHHCCCCCCCCCCCC	51.96	23503661
1286	Ubiquitination	HSDELNCPVCSESQF CCCCCCCCCCCHHHE	29.13	23000965
1292	Ubiquitination	CPVCSESQFQCASGQ CCCCCHHHEEECCCC	28.51	23000965
1326	Ubiquitination	EKNCEVLCLIDQFRC CCCCEEEEEEEEEEC	3.65	23503661
1394	S-palmitoylation	SGTVYFICQRMLCPR CCHHHHHHHHHHCCC	1.18	18378904
1399	S-palmitoylation	FICQRMLCPRMKGDG HHHHHHHCCCCCCCC	1.15	18378904
1403	Ubiquitination	RMLCPRMKGDGETMT HHHCCCCCCCCCCCC	55.95	23000965
1408	Phosphorylation	RMKGDGETMTNDYVV CCCCCCCCCCCCEEE	34.52	27470641
1410	Phosphorylation	KGDGETMTNDYVVHG CCCCCCCCCCEEEEC	32.15	27470641
1413	Phosphorylation	GETMTNDYVVHGPAS CCCCCCCEEEECCCC	13.36	27642862
1420	Phosphorylation	YVVHGPASVPLGYVP EEEECCCCCCCCCCC	27.66	16513652
1425	Phosphorylation	PASVPLGYVPHPSSL CCCCCCCCCCCHHHC	20.63	27642862
1430	Phosphorylation	LGYVPHPSSLSGSLP CCCCCCHHHCCCCCC	40.66	16513652
1431	Phosphorylation	GYVPHPSSLSGSLPG CCCCCHHHCCCCCCC	30.88	22817900
1435	Phosphorylation	HPSSLSGSLPGMSRG CHHHCCCCCCCCCCC	28.19	27470641
1440	Phosphorylation	SGSLPGMSRGKSMIS CCCCCCCCCCHHHHH	43.74	27470641
1443	Ubiquitination	LPGMSRGKSMISSLS CCCCCCCHHHHHHCE	35.42	23000965
1444	Phosphorylation	PGMSRGKSMISSLSI CCCCCCHHHHHHCEE	24.95	24719451
1455	Phosphorylation	SLSIMGGSSGPPYDR HCEECCCCCCCCCCC	26.79	-
1460	Phosphorylation	GGSSGPPYDRAHVTG CCCCCCCCCCCCCCC	22.61	25884760
1466	Phosphorylation	PYDRAHVTGASSSSS CCCCCCCCCCCCCCC	19.70	23532336
1469	Phosphorylation	RAHVTGASSSSSSST CCCCCCCCCCCCCCC	31.90	23312004
1470	Phosphorylation	AHVTGASSSSSSSTK CCCCCCCCCCCCCCC	33.43	23312004
1471	Phosphorylation	HVTGASSSSSSSTKG CCCCCCCCCCCCCCC	31.57	23312004
1472	Phosphorylation	VTGASSSSSSSTKGT CCCCCCCCCCCCCCC	35.87	23312004
1473	Phosphorylation	TGASSSSSSSTKGTY CCCCCCCCCCCCCCC	30.20	23312004
1474	Phosphorylation	GASSSSSSSTKGTYF CCCCCCCCCCCCCCC	43.93	23312004
1475	Phosphorylation	ASSSSSSSTKGTYFP CCCCCCCCCCCCCCC	35.77	22322096
1476	Phosphorylation	SSSSSSSTKGTYFPA CCCCCCCCCCCCCCE	35.13	22322096
1477	Ubiquitination	SSSSSSTKGTYFPAI CCCCCCCCCCCCCEE	51.72	23503661
1479	Phosphorylation	SSSSTKGTYFPAILN CCCCCCCCCCCEEEC	24.44	22322096
1480	Phosphorylation	SSSTKGTYFPAILNP CCCCCCCCCCEEECC	19.08	22322096
1490	Phosphorylation	AILNPPPSPATERSH EEECCCCCCCCCCCE	32.70	30266825
1493	Phosphorylation	NPPPSPATERSHYTM CCCCCCCCCCCEEEE	35.00	22322096
1496	Phosphorylation	PSPATERSHYTMEFG CCCCCCCCEEEEEEC	18.02	-
1498	Phosphorylation	PATERSHYTMEFGYS CCCCCCEEEEEECCC	14.72	27642862
1499	Phosphorylation	ATERSHYTMEFGYSS CCCCCEEEEEECCCC	12.56	23312004
1504	Phosphorylation	HYTMEFGYSSNSPST EEEEEECCCCCCCCC	17.78	23312004
1505	Phosphorylation	YTMEFGYSSNSPSTH EEEEECCCCCCCCCC	24.35	29214152
1506	Phosphorylation	TMEFGYSSNSPSTHR EEEECCCCCCCCCCC	32.61	22617229
1508	Phosphorylation	EFGYSSNSPSTHRSY EECCCCCCCCCCCCC	23.36	26055452
1510	Phosphorylation	GYSSNSPSTHRSYSY CCCCCCCCCCCCCCC	36.34	29523821
1511	Phosphorylation	YSSNSPSTHRSYSYR CCCCCCCCCCCCCCC	25.37	29523821
1514	Phosphorylation	NSPSTHRSYSYRPYS CCCCCCCCCCCCCCE	15.72	27642862
1515	Phosphorylation	SPSTHRSYSYRPYSY CCCCCCCCCCCCCEE	15.07	25884760
1516	Phosphorylation	PSTHRSYSYRPYSYR CCCCCCCCCCCCEEC	18.86	27422710
1517	Phosphorylation	STHRSYSYRPYSYRH CCCCCCCCCCCEECC	13.84	28555341
1518	Methylation	THRSYSYRPYSYRHF CCCCCCCCCCEECCC	20.10	81450677
1520	Phosphorylation	RSYSYRPYSYRHFAP CCCCCCCCEECCCCC	14.88	25884760
1521	Phosphorylation	SYSYRPYSYRHFAPP CCCCCCCEECCCCCC	20.55	25884760
1522	Phosphorylation	YSYRPYSYRHFAPPT CCCCCCEECCCCCCC	11.41	22817900
1529	Phosphorylation	YRHFAPPTTPCSTDV ECCCCCCCCCCCCCC	42.16	27642862
1530	Phosphorylation	RHFAPPTTPCSTDVC CCCCCCCCCCCCCCC	28.24	27642862
1533	Phosphorylation	APPTTPCSTDVCDSD CCCCCCCCCCCCCCC	28.92	27642862
1539	Phosphorylation	CSTDVCDSDYAPSRR CCCCCCCCCCCCCCC	27.65	28796482
1541	Phosphorylation	TDVCDSDYAPSRRMT CCCCCCCCCCCCCCC	25.10	25884760
1544	Phosphorylation	CDSDYAPSRRMTSVA CCCCCCCCCCCCEEE	25.09	28796482
1548	Phosphorylation	YAPSRRMTSVATAKG CCCCCCCCEEEECCC	20.45	21406690
1554	Ubiquitination	MTSVATAKGYTSDLN CCEEEECCCCCCCCC	48.36	23000965
1556	Phosphorylation	SVATAKGYTSDLNYD EEEECCCCCCCCCCC	11.45	27732954
1557	Phosphorylation	VATAKGYTSDLNYDS EEECCCCCCCCCCCC	25.16	27732954
1558	Phosphorylation	ATAKGYTSDLNYDSE EECCCCCCCCCCCCC	31.45	27732954
1562	Phosphorylation	GYTSDLNYDSEPVPP CCCCCCCCCCCCCCC	28.30	27732954
1564	Phosphorylation	TSDLNYDSEPVPPPP CCCCCCCCCCCCCCC	33.18	27732954
1572	Phosphorylation	EPVPPPPTPRSQYLS CCCCCCCCCHHHCCC	36.79	21815630
1575	Phosphorylation	PPPPTPRSQYLSAEE CCCCCCHHHCCCHHH	25.12	27732954
1577	Phosphorylation	PPTPRSQYLSAEENY CCCCHHHCCCHHHCC	12.13	22817900
1579	Phosphorylation	TPRSQYLSAEENYES CCHHHCCCHHHCCCC	28.80	27732954
1584	Phosphorylation	YLSAEENYESCPPSP CCCHHHCCCCCCCCC	16.70	27259358
1586	Phosphorylation	SAEENYESCPPSPYT CHHHCCCCCCCCCCC	22.89	27732954
1590	Phosphorylation	NYESCPPSPYTERSY CCCCCCCCCCCCCCC	18.71	30576142
1592	Phosphorylation	ESCPPSPYTERSYSH CCCCCCCCCCCCCCC	26.10	30175587
1593	Phosphorylation	SCPPSPYTERSYSHH CCCCCCCCCCCCCCC	28.45	22210691
1607	Phosphorylation	HLYPPPPSPCTDSS- CCCCCCCCCCCCCC-	38.08	30576142
1610	Phosphorylation	PPPPSPCTDSS---- CCCCCCCCCCC----	42.15	23836654
1612	Phosphorylation	PPSPCTDSS------ CCCCCCCCC------	21.57	27732954
1613	Phosphorylation	PSPCTDSS------- CCCCCCCC-------	47.23	27732954

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
1420	S	Phosphorylation	Kinase	CK1	-	Uniprot
1420	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
1420	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
1430	S	Phosphorylation	Kinase	CK1	-	Uniprot
1430	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
1431	S	Phosphorylation	Kinase	CSNK1E	P49674	GPS
1479	T	Phosphorylation	Kinase	CSNK1G1	Q9HCP0	GPS
1490	S	Phosphorylation	Kinase	GRK5	P34947	Uniprot
1490	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
1490	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
1490	S	Phosphorylation	Kinase	CK1A	P48729	PSP
1490	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
1490	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
1490	S	Phosphorylation	Kinase	GRK6	P43250	Uniprot
1490	S	Phosphorylation	Kinase	CDK14	O94921	Uniprot
1493	T	Phosphorylation	Kinase	CSNK1A1	P48729	GPS
1493	T	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
1493	T	Phosphorylation	Kinase	CK1	-	Uniprot
1544	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
1548	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
1572	T	Phosphorylation	Kinase	CK1A	P48729	PSP
1572	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
1572	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
1572	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
1607	S	Phosphorylation	Kinase	CK1A	P48729	PSP
1607	S	Phosphorylation	Kinase	GSK3A	P49840	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:28966723

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1479	T	Phosphorylation	17569865
Phosphorylated, in vitro, by casein kinase I on Thr-1479.
1490	S	Phosphorylation	16341017
Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to regulation of the Wnt signaling pathway during the cell cycle.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of LRP6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPC1_HUMAN	NPC1	physical	18948618
ZNRF3_HUMAN	ZNRF3	physical	22575959
WNT3A_HUMAN	WNT3A	physical	19910923
WNT5A_HUMAN	WNT5A	physical	19910923
LRRK2_HUMAN	LRRK2	physical	22899650
AXIN1_HUMAN	AXIN1	physical	16890161
CTNB1_HUMAN	CTNNB1	physical	16890161
GSK3B_HUMAN	GSK3B	physical	16890161
CAV1_HUMAN	CAV1	physical	16890161
DKK1_HUMAN	DKK1	physical	15035989
GSK3B_HUMAN	GSK3B	physical	19107203
AXIN1_HUMAN	AXIN1	physical	19107203
WNT1_HUMAN	WNT1	physical	11448771
DKK1_HUMAN	DKK1	physical	11448771
PEDF_HUMAN	SERPINF1	physical	21576363
GAS8_HUMAN	GAS8	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610947	Coronary artery disease, autosomal dominant, 2 (ADCAD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LRP6_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural basis of Wnt signaling inhibition by Dickkopf binding toLRP5/6."; Ahn V.E., Chu M.L., Choi H.J., Tran D., Abo A., Weis W.I.; Dev. Cell 21:862-873(2011). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 630-1246 IN COMPLEX WITHDKK1, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-692; ASN-859;ASN-865; ASN-926 AND ASN-1039.	22000856 [Abstract]
Palmitoylation
Reference	PubMed
"Palmitoylation and ubiquitination regulate exit of the Wnt signalingprotein LRP6 from the endoplasmic reticulum."; Abrami L., Kunz B., Iacovache I., van der Goot F.G.; Proc. Natl. Acad. Sci. U.S.A. 105:5384-5389(2008). Cited for: PALMITOYLATION AT CYS-1394 AND CYS-1399, UBIQUITINATION AT LYS-1403,SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1394 AND CYS-1399.	18378904 [Abstract]
Phosphorylation
Reference	PubMed
"G Protein-coupled receptor kinases phosphorylate LRP6 in the Wntpathway."; Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G.,Lefkowitz R.J., Chen W.; J. Biol. Chem. 284:35040-35048(2009). Cited for: PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490, ANDFUNCTION.	19801552 [Abstract]
"Cell cycle control of wnt receptor activation."; Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E.,Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.; Dev. Cell 17:788-799(2009). Cited for: DOMAIN PPPSP MOTIF, AND PHOSPHORYLATION AT SER-1490.	20059949 [Abstract]
"Analysis of endogenous LRP6 function reveals a novel feedbackmechanism by which Wnt negatively regulates its receptor."; Khan Z., Vijayakumar S., de la Torre T.V., Rotolo S., Bafico A.; Mol. Cell. Biol. 27:7291-7301(2007). Cited for: GLYCOSYLATION, PHOSPHORYLATION AT SER-1490, INTERACTION WITH AXIN1,HOMODIMERIZATION, INDUCTION, AND SUBCELLULAR LOCATION.	17698587 [Abstract]
"Negative regulation of LRP6 function by casein kinase I epsilonphosphorylation."; Swiatek W., Kang H., Garcia B.A., Shabanowitz J., Coombs G.S.,Hunt D.F., Virshup D.M.; J. Biol. Chem. 281:12233-12241(2006). Cited for: PHOSPHORYLATION AT SER-1420 AND SER-1430, FUNCTION, INTERACTION WITHCSNKIE AND AXIN1, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-1420 ANDSER-1430.	16513652 [Abstract]
"A dual-kinase mechanism for Wnt co-receptor phosphorylation andactivation."; Zeng X., Tamai K., Doble B., Li S., Huang H., Habas R., Okamura H.,Woodgett J., He X.; Nature 438:873-877(2005). Cited for: PHOSPHORYLATION OF PPPSP MOTIFS, PHOSPHORYLATION AT SER-1490 ANDTHR-1493, AND FUNCTION.	16341017 [Abstract]
"Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6phosphorylation."; Bilic J., Huang Y.L., Davidson G., Zimmermann T., Cruciat C.M.,Bienz M., Niehrs C.; Science 316:1619-1622(2007). Cited for: PHOSPHORYLATION AT THR-1479, INTERACTION OF AXIN1, SUBUNIT, ANDSUBCELLULAR LOCATION.	17569865 [Abstract]
Ubiquitylation
Reference	PubMed
"Palmitoylation and ubiquitination regulate exit of the Wnt signalingprotein LRP6 from the endoplasmic reticulum."; Abrami L., Kunz B., Iacovache I., van der Goot F.G.; Proc. Natl. Acad. Sci. U.S.A. 105:5384-5389(2008). Cited for: PALMITOYLATION AT CYS-1394 AND CYS-1399, UBIQUITINATION AT LYS-1403,SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1394 AND CYS-1399.	18378904 [Abstract]

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